Cfb Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
--- [@molecular2018] title: CFB Protein — Complement Factor B [@protein2017] ---<div id="protein-infobox" class="infobox infobox-protein"></div> [@genetic2017]
Structure
Complement Factor B (CFB) is a single-chain glycoprotein that belongs to the [complement system](/entities/complement-system) serine protease family. It consists of: [@neuroinflammation2015]
Ba fragment (30 kDa): N-terminal domain, released upon activation
Bb fragment (55 kDa): C-terminal serine protease domain, remains bound to C3b
The protein contains: [@cellular2018]
Three short consensus repeats (SCR): N-terminal Ba region for C3b binding
Von Willebrand factor type A (vWF-A) domain: Mediates protein-protein interactions
Serine protease (SP) domain: Catalytic domain with His-Asp-Ser triad [1]
Crystal structures of CFB have revealed conformational changes upon C3b binding that position the Bb serine protease domain for activation [2]. [@therapeutic2017]
Normal Function
In the classical/lectin/alternative complement pathways, CFB plays a central role: [@biomarkers2016]
...
CFB Protein — Complement Factor B
Introduction
Cfb Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
--- [@molecular2018] title: CFB Protein — Complement Factor B [@protein2017] ---<div id="protein-infobox" class="infobox infobox-protein"></div> [@genetic2017]
Structure
Complement Factor B (CFB) is a single-chain glycoprotein that belongs to the [complement system](/entities/complement-system) serine protease family. It consists of: [@neuroinflammation2015]
Ba fragment (30 kDa): N-terminal domain, released upon activation
Bb fragment (55 kDa): C-terminal serine protease domain, remains bound to C3b
The protein contains: [@cellular2018]
Three short consensus repeats (SCR): N-terminal Ba region for C3b binding
Von Willebrand factor type A (vWF-A) domain: Mediates protein-protein interactions
Serine protease (SP) domain: Catalytic domain with His-Asp-Ser triad [1]
Crystal structures of CFB have revealed conformational changes upon C3b binding that position the Bb serine protease domain for activation [2]. [@therapeutic2017]
Normal Function
In the classical/lectin/alternative complement pathways, CFB plays a central role: [@biomarkers2016]
Alternative pathway activation: CFB spontaneously cleaves C3 (tick-over) to form C3(H2O)
C3 convertase formation: CFB binds to C3b and is cleaved by Factor D to form C3bBb (C3 convertase)
The study of Cfb Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.